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Journal ArticleDOI

Histone modifications in transcriptional regulation.

Shelley L. Berger
- 01 Apr 2002 - 
- Vol. 12, Iss: 2, pp 142-148
TLDR
Research in the past two years reveals these modifications to consist of phosphorylation, methylation and ubiquitination, in addition to the better-characterized acetylation, which argues persuasively for the existence of a histone code.
About
This article is published in Current Opinion in Genetics & Development.The article was published on 2002-04-01. It has received 1215 citations till now. The article focuses on the topics: Histone code & Histone-modifying enzymes.

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Citations
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Journal ArticleDOI

Intrinsically unstructured proteins and their functions.

TL;DR: Many gene sequences in eukaryotic genomes encode entire proteins or large segments of proteins that lack a well-structured three-dimensional fold, whereas others constitute flexible linkers that have a role in the assembly of macromolecular arrays.
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Combinatorial patterns of histone acetylations and methylations in the human genome

TL;DR: The data suggest that a large number of histone modifications may act cooperatively to prepare chromatin for transcriptional activation and be associated with promoters and enhancers.
Journal ArticleDOI

TGF-β: the master regulator of fibrosis

TL;DR: Studies over the past 5 years have identified additional mechanisms that regulate the action of TGF-β1/Smad signalling in fibrosis, including short and long noncoding RNA molecules and epigenetic modifications of DNA and histone proteins.
Journal ArticleDOI

Estrogen Receptor-α Directs Ordered, Cyclical, and Combinatorial Recruitment of Cofactors on a Natural Target Promoter

TL;DR: A comprehensive picture of events resulting in transcriptional activation of a gene is provided, through evaluating the estrogen receptor-alpha (NR3A1) target pS2 gene promoter in MCF-7 cells, which implies that transcriptionalactivation is a cyclical process that requires both activating and repressive epigenetic processes.
Journal ArticleDOI

Substrate and Functional Diversity of Lysine Acetylation Revealed by a Proteomics Survey

TL;DR: This study reveals previously unappreciated roles for lysine acetylation in the regulation of diverse cellular pathways outside of the nucleus, including many longevity regulators and metabolism enzymes.
References
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Journal ArticleDOI

The language of covalent histone modifications.

TL;DR: It is proposed that distinct histone modifications, on one or more tails, act sequentially or in combination to form a ‘histone code’ that is, read by other proteins to bring about distinct downstream events.
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Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins.

TL;DR: It is shown that mammalian methyltransferases that selectively methylate histone H3 on lysine 9 (Suv39h HMTases) generate a binding site for HP1 proteins—a family of heterochromatic adaptor molecules implicated in both gene silencing and supra-nucleosomal chromatin structure.
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Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain.

TL;DR: A stepwise model for the formation of a transcriptionally silent heterochromatin is provided: SUV39H1 places a ‘methyl marker’ on histone H3, which is then recognized by HP1 through its chromo domain, which may also explain the stable inheritance of theheterochromatic state.
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Regulation of chromatin structure by site-specific histone H3 methyltransferases

TL;DR: A functional interdependence of site-specific H3 tail modifications is revealed and a dynamic mechanism for the regulation of higher-order chromatin is suggested.
Journal ArticleDOI

Acetylation of Histones and Transcription-Related Factors

TL;DR: This work detail these known factor acetyltransferase (FAT) substrates and the demonstrated or potential roles of their acetylation in transcriptional processes.
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